Difference between revisions of "YpwA"
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3HQ2 3HQ2] [http://www.ncbi.nlm.nih.gov/sites/entrez/19544567 PubMed] | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3HQ2 3HQ2] [http://www.ncbi.nlm.nih.gov/sites/entrez/19544567 PubMed] | ||
| − | * ''' | + | * '''UniProt:''' [http://www.uniprot.org/uniprot/P50848 P50848] |
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU22080] | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU22080] | ||
Revision as of 13:15, 20 July 2009
- Description: carboxypeptidase, metalloprotease
| Gene name | ypwA |
| Synonyms | |
| Essential | no |
| Product | M32 carboxypeptidase |
| Function | unknown |
| MW, pI | 58 kDa, 4.77 |
| Gene length, protein length | 1503 bp, 501 aa |
| Immediate neighbours | xpt, kdgT |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU22080
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: M32 carboxypeptidase
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions: dimer PubMed
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P50848
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Marianne M Lee, Clara E Isaza, James D White, Rita P-Y Chen, George F-C Liang, Hannah T-F He, Sunney I Chan, Michael K Chan
Insight into the substrate length restriction of M32 carboxypeptidases: characterization of two distinct subfamilies.
Proteins: 2009, 77(3);647-57
[PubMed:19544567]
[WorldCat.org]
[DOI]
(I p)
